Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]

Recent accumulation of sequence and structural data, in conjunction with systematical classification into a set of families, has significantly advanced our understanding of diverse and specific protein functions. Analysis and interpretation of protein family data requires comprehensive sequence and...

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Main Authors: Miki Asano, Shunta Ide, Atsushi Kamata, Kiyohiro Takahasi, Tetsuji Okada
Format: Article
Language:English
Published: F1000 Research Ltd 2016-04-01
Series:F1000Research
Subjects:
Online Access:http://f1000research.com/articles/5-165/v2
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spelling doaj-cf737700a1414d2a9985ee7f945a90792020-11-25T03:06:38ZengF1000 Research LtdF1000Research2046-14022016-04-01510.12688/f1000research.7920.29078Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]Miki Asano0Shunta Ide1Atsushi Kamata2Kiyohiro Takahasi3Tetsuji Okada4Department of Life Science, Gakushuin University, Tokyo, JapanDepartment of Life Science, Gakushuin University, Tokyo, JapanDepartment of Life Science, Gakushuin University, Tokyo, JapanDepartment of Life Science, Gakushuin University, Tokyo, JapanDepartment of Life Science, Gakushuin University, Tokyo, JapanRecent accumulation of sequence and structural data, in conjunction with systematical classification into a set of families, has significantly advanced our understanding of diverse and specific protein functions. Analysis and interpretation of protein family data requires comprehensive sequence and structural alignments. Here, we present a simple scheme for analyzing a set of experimental structures of a given protein or family of proteins, using microbial rhodopsins as an example. For a data set comprised of around a dozen highly similar structures to each other (overall pairwise root-mean-squared deviation < 2.3 Å), intramolecular distance scoring analysis yielded valuable information with respect to structural properties, such as differences in the relative variability of transmembrane helices. Furthermore, a comparison with recent results for G protein-coupled receptors demonstrates how the results of the present analysis can be interpreted and effectively utilized for structural characterization of diverse protein families in general.http://f1000research.com/articles/5-165/v2BioinformaticsProtein Chemistry & Proteomics
collection DOAJ
language English
format Article
sources DOAJ
author Miki Asano
Shunta Ide
Atsushi Kamata
Kiyohiro Takahasi
Tetsuji Okada
spellingShingle Miki Asano
Shunta Ide
Atsushi Kamata
Kiyohiro Takahasi
Tetsuji Okada
Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]
F1000Research
Bioinformatics
Protein Chemistry & Proteomics
author_facet Miki Asano
Shunta Ide
Atsushi Kamata
Kiyohiro Takahasi
Tetsuji Okada
author_sort Miki Asano
title Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]
title_short Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]
title_full Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]
title_fullStr Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]
title_full_unstemmed Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]
title_sort sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]
publisher F1000 Research Ltd
series F1000Research
issn 2046-1402
publishDate 2016-04-01
description Recent accumulation of sequence and structural data, in conjunction with systematical classification into a set of families, has significantly advanced our understanding of diverse and specific protein functions. Analysis and interpretation of protein family data requires comprehensive sequence and structural alignments. Here, we present a simple scheme for analyzing a set of experimental structures of a given protein or family of proteins, using microbial rhodopsins as an example. For a data set comprised of around a dozen highly similar structures to each other (overall pairwise root-mean-squared deviation < 2.3 Å), intramolecular distance scoring analysis yielded valuable information with respect to structural properties, such as differences in the relative variability of transmembrane helices. Furthermore, a comparison with recent results for G protein-coupled receptors demonstrates how the results of the present analysis can be interpreted and effectively utilized for structural characterization of diverse protein families in general.
topic Bioinformatics
Protein Chemistry & Proteomics
url http://f1000research.com/articles/5-165/v2
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